On the relationship between the hill coefficients for steady-state and transient kinetic data: A criterion for concerted transitions in allosteric proteins

Amnon Horovitz, Ofer Yifrach

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

A frequently used measure for the extent of cooperativity in ligand binding by allosteric proteins is the Hill coefficient. Hill coefficients can be measured for steady-state kinetic data and also for transient kinetic data. Here, the relationship between the two types of Hill coefficients is analysed. It is shown that a value of 1 for the ratio of the two Hill coefficients is a test for a concerted ligand-induced transition between two conformations of the protein, in accordance with the Monod-Wyman-Changeux model. A value of 1 for this ratio has recently been observed for a series of chaperonin GroEL mutants suggesting that ATP-induced allosteric transitions in this protein are concerted. (C) 2000 Society for Mathematical Biology.

Original languageEnglish
Pages (from-to)241-246
Number of pages6
JournalBulletin of Mathematical Biology
Volume62
Issue number2
DOIs
StatePublished - 1 Jan 2000
Externally publishedYes

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